BACSU:RIR1

Species (Taxon ID)	Bacillus subtilis (strain 168). (224308)
Gene Name(s)	nrdE (synonyms: nrdA)
Protein Name(s)	Ribonucleoside-diphosphate reductase subunit alpha Ribonucleotide reductase large subunit
External Links
UniProt	P50620
EMBL	Z68500 AL009126
PIR	B69667
RefSeq	NP_389620.1
ProteinModelPortal	P50620
SMR	P50620
STRING	224308.BSU17380
PaxDb	P50620
PRIDE	P50620
EnsemblBacteria	CAB13622
GeneID	940091
KEGG	bsu:BSU17380
PATRIC	18975287
GenoList	BSU17380
eggNOG	COG0209
HOGENOM	HOG000246165
InParanoid	P50620
KO	K00525
OMA	TCSAPRQ
OrthoDB	EOG6J48HC
PhylomeDB	P50620
BioCyc	BSUB:BSU17380-MONOMER
UniPathway	UPA00326
Proteomes	UP000001570
GO	GO:0005524 GO:0004748 GO:0006260
InterPro	IPR013346 IPR026459 IPR000788 IPR013509 IPR013554 IPR008926
Pfam	PF02867 PF00317 PF08343
PRINTS	PR01183
SUPFAM	SSF48168
TIGRFAMs	TIGR02506 TIGR04170
PROSITE	PS00089

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Extension	Notes	Status
	GO:0004748	ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor	PMID:8969495	ECO:0000315			F		This paper follows the studies in another article (PMID 4627024) which I don't have access to read past the beginning results and the abstract. This previous article used a temperature sensitive mutant ts-167 to determine the function of the nrdEF locus. That paper determined the function by analyzing the pool of dNTP present at the restrictive temperature. dCTP and dATP were not apparent at these restrictive temperatures. The reference listed above (PMID 8969495) used phylogeny and sequencing to determine that Enterobacteria favor the use of nrdAB loci, whereas Bacilus subtils has evolved to use nrdEF. They also used clone pMP25.8 to rescue the temperature sensitive mutant, and later sequenced the nrdE mutant to determine there were 2 neutral mutations and 1 mutation that led to the lethality of the temperature sensitive mutant. They concluded that this mutation was the cause for the loss of function of the NrdE protein. The mutant lethality due to the loss of dCTP and dATP synthesis provides evidenct that this gene is responsible for the essential enzyme responsible for reductase activity for the respective ribonucleoside-diphosphates.	complete CACAO 10873
involved_in	GO:0009263	deoxyribonucleotide biosynthetic process		ECO:0000318	biological aspect of ancestor evidence used in manual assertion	EcoGene:EG10660 EcoGene:EG20257 MGI:MGI:98180 PANTHER:PTN000171388 SGD:S000000872 SGD:S000001328 UniProtKB:P9WH75	P		Seeded From UniProt	complete
part_of	GO:0005971	ribonucleoside-diphosphate reductase complex		ECO:0000318	biological aspect of ancestor evidence used in manual assertion	EcoGene:EG10660 EcoGene:EG20257 MGI:MGI:98180 PANTHER:PTN000171388 PomBase:SPAC1F7.05 SGD:S000000872 UniProtKB:P9WH75 UniProtKB:Q9I4I1	C		Seeded From UniProt	complete
enables	GO:0004748	ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor		ECO:0000318	biological aspect of ancestor evidence used in manual assertion	EcoGene:EG10660 EcoGene:EG20257 MGI:MGI:98180 PANTHER:PTN000171388 SGD:S000000872 SGD:S000001328 UniProtKB:P9WH75 UniProtKB:Q08698	F		Seeded From UniProt	complete
enables	GO:0004748	ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR013509	F		Seeded From UniProt	complete
enables	GO:0005524	ATP binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR013509	F		Seeded From UniProt	complete
involved_in	GO:0006260	DNA replication	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR000788 InterPro:IPR013509	P		Seeded From UniProt	complete
involved_in	GO:0055114	oxidation-reduction process	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR000788 InterPro:IPR013346 InterPro:IPR013509	P		Seeded From UniProt	complete
enables	GO:0004748	ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor	GO_REF:0000003	ECO:0000501	evidence used in automatic assertion	EC:1.17.4.1	F		Seeded From UniProt	complete
enables	GO:0003824	catalytic activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0021	F		Seeded From UniProt	complete
involved_in	GO:0006260	DNA replication	GO_REF:0000037 GO_REF:0000041	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0235 UniPathway:UPA00326	P		Seeded From UniProt	complete
enables	GO:0005524	ATP binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0067	F		Seeded From UniProt	complete
involved_in	GO:0055114	oxidation-reduction process	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0560	P		Seeded From UniProt	complete
involved_in	GO:0008152	metabolic process	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0021	P		Seeded From UniProt	complete
enables	GO:0016491	oxidoreductase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0560	F		Seeded From UniProt	complete
enables	GO:0000166	nucleotide binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0547	F		Seeded From UniProt	complete
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References

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